Structure of the Arabidopsis thaliana TOP2 oligopeptidase.
Structure of the Arabidopsis thaliana TOP2 oligopeptidase.
复制标题
拟南芥 TOP2 寡肽酶的结构。
DOI：
10.1107/s2053230x14006128
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Tong,Liang
中科院分区：
文献类型：
--
作者：
Wang,Ruiying;Rajagopalan,Krithika;Sadre-Bazzaz,Kianoush;Moreau,Magali;Klessig,DanielF;Tong,Liang
蒂美特寡肽酶 (TOP) 是一种锌依赖性金属肽酶。最近的研究表明，拟南芥 TOP1 和 TOP2 是水杨酸 (SA) 结合的靶标，并参与 SA 介导的植物先天免疫。拟南芥 TOP2 的晶体结构已在 3.0 Å 分辨率下确定。与人类 TOP 结构的比较显示出良好的整体结构保守性，特别是在活性位点区域，尽管其序列保守性较弱。将蛋白质样品与光激活的 SA 类似物 4-叠氮基-SA 一起孵育，并在结晶前暴露于紫外线照射。然而，根据 X 射线衍射数据，没有确凿的证据证明 SA 的结合。需要进一步的研究来阐明SA如何调节拟南芥TOP1和TOP2活性的分子机制。
Thimet oligopeptidase (TOP) is a zinc-dependent metallopeptidase. Recent studies suggest that Arabidopsis thaliana TOP1 and TOP2 are targets for salicylic acid (SA) binding and participate in SA-mediated plant innate immunity. The crystal structure of A. thaliana TOP2 has been determined at 3.0 Å resolution. Comparisons to the structure of human TOP revealed good overall structural conservation, especially in the active-site region, despite their weak sequence conservation. The protein sample was incubated with the photo-activated SA analog 4-azido-SA and exposed to UV irradiation before crystallization. However, there was no conclusive evidence for the binding of SA based on the X-ray diffraction data. Further studies are needed to elucidate the molecular mechanism of how SA regulates the activity of A. thaliana TOP1 and TOP2.